A Second Pectin Lyase Gene(pel2) from Aspergillus oryzae KBN616. Its Sequence Analysis and Overexpression, and Characterization of the Gene Products.

Kitamoto, Noriyuki; Yoshino-Yasuda, Shoko; Ohmiya, Kunio; Tsukagoshi, Norihiro

doi:10.1263/jbb.91.378

Cited by 11 publications

(4 citation statements)

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“…Most of the available information about fungal PNLs and their corresponding encoding genes has been obtained from saprophytic/opportunistic fungi such as Aspergillus niger [16-19], A. orizae [20,21], A. fumigatus [22], Penicillium griseoroseum [23], P. occitanis [24] and to a lesser extent from the phytopathogenic fungi Glomerella cingulata [25] and C. gloeosporioides [26]. …”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of a pectin lyase gene from Colletotrichum lindemuthianumand comparative phylogenetic/structural analyses with genes from phytopathogenic and saprophytic/opportunistic microorganisms

et al. 2011

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BackgroundMicroorganisms produce cell-wall-degrading enzymes as part of their strategies for plant invasion/nutrition. Among these, pectin lyases (PNLs) catalyze the depolymerization of esterified pectin by a β-elimination mechanism. PNLs are grouped together with pectate lyases (PL) in Family 1 of the polysaccharide lyases, as they share a conserved structure in a parallel β-helix. The best-characterized fungal pectin lyases are obtained from saprophytic/opportunistic fungi in the genera Aspergillus and Penicillium and from some pathogens such as Colletotrichum gloeosporioides.The organism used in the present study, Colletotrichum lindemuthianum, is a phytopathogenic fungus that can be subdivided into different physiological races with different capacities to infect its host, Phaseolus vulgaris. These include the non-pathogenic and pathogenic strains known as races 0 and 1472, respectively.ResultsHere we report the isolation and sequence analysis of the Clpnl2 gene, which encodes the pectin lyase 2 of C. lindemuthianum, and its expression in pathogenic and non-pathogenic races of C. lindemuthianum grown on different carbon sources. In addition, we performed a phylogenetic analysis of the deduced amino acid sequence of Clpnl2 based on reported sequences of PNLs from other sources and compared the three-dimensional structure of Clpnl2, as predicted by homology modeling, with those of other organisms. Both analyses revealed an early separation of bacterial pectin lyases from those found in fungi and oomycetes. Furthermore, two groups could be distinguished among the enzymes from fungi and oomycetes: one comprising enzymes from mostly saprophytic/opportunistic fungi and the other formed mainly by enzymes from pathogenic fungi and oomycetes. Clpnl2 was found in the latter group and was grouped together with the pectin lyase from C. gloeosporioides.ConclusionsThe Clpnl2 gene of C. lindemuthianum shares the characteristic elements of genes coding for pectin lyases. A time-course analysis revealed significant differences between the two fungal races in terms of the expression of Clpnl2 encoding for pectin lyase 2. According to the results, pectin lyases from bacteria and fungi separated early during evolution. Likewise, the enzymes from fungi and oomycetes diverged in accordance with their differing lifestyles. It is possible that the diversity and nature of the assimilatory carbon substrates processed by these organisms played a determinant role in this phenomenon.

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Section: Introductionmentioning

confidence: 99%

Cloning and characterization of a pectin lyase gene from Colletotrichum lindemuthianumand comparative phylogenetic/structural analyses with genes from phytopathogenic and saprophytic/opportunistic microorganisms

et al. 2011

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“…This variation in the isoforms of extracellular enzymes can be attributed to many factors, such as the presence of several genes, different degrees of glycosylation, posttranscriptional processing, or proteolysis after secretion [14, 30]. Multiple isoforms of secreted pectinases are usually obtained in fungal culture media [11, 22, 31, 32] since the infection of host living tissue by a pathogen and colonization of plant cells decaying by saprophytic microorganisms is facilitated if a sufficient quantity and a number of isoform types of pectinase are produced [33].…”

Section: Resultsmentioning

confidence: 99%

Production of Pectate Lyase byPenicillium viridicatum RFC3in Solid-State and Submerged Fermentation

Ferreira

Silva

et al. 2010

International Journal of Microbiology

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Pectate lyase (PL) was produced by the filamentous fungus Penicillium viridicatum RFC3 in solid-state cultures of a mixture of orange bagasse and wheat bran (1 : 1 w/w), or orange bagasse, wheat bran and sugarcane bagasse (1 : 1 : 0.5 w/w), and in a submerged liquid culture with orange bagasse and wheat bran (3%) as the carbon source. PL production was highest (1,500 U mL−1 or 300 Ug−1 of substrate) in solid-state fermentation (SSF) on wheat bran and orange bagasse at 96 hours. PL production in submerged fermentation (SmF) was influenced by the initial pH of the medium. With the initial pH adjusted to 4.5, 5.0, and 5.5, the peak activity was observed after 72, 48, and 24 hours of fermentation, respectively, when the pH of the medium reached the value 5.0. PL from SSF and SmF were loaded on Sephadex-G75 columns and six activity peaks were obtained from crude enzyme from SSF and designated PL I, II, III, IV, V, and VI, while five peaks were obtained from crude enzyme from SmF and labeled PL I′, II′, III′, IV′, and VII′. Crude enzyme and fraction III from each fermentative process were tested further. The optimum pH for crude PL from either process was 5.5, while that for PL III was 8.0. The maximum activity of enzymes from SSF was observed at 35°C, but crude enzyme was more thermotolerant than PL III, maintaining its maximum activity up to 45°C. Crude enzyme from SmF and PL III′ showed thermophilic profiles of activity, with maximum activity at 60 and 55°C, respectively. In the absence of substrate, the crude enzyme from SSF was stable over the pH range 3.0–10.0 and PL III was most stable in the pH range 4.0–7.0. Crude enzyme from SmF retained 70%–80% of its maximum activity in the acid-neutral pH range (4.0–7.0), but PIII showed high stability at alkaline pH (7.5–9.5). PL from SSF was more thermolabile than that from SmF. The latter maintained 60% of its initial activity after 1 h at 55°C. The differing behavior of the enzymes with respect to pH and temperature suggests that they are different isozymes.

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“…The presence of several binding sites for PacC suggests a similar regulation to PNL genes from A . niger , Glomerella cingulata (teleomorph/; C. gloeosporioides ) and Aspergillus oryzae (Templeton et al 1994; Benen et al 1996; Kitamoto et al . 2001a,b), that are better expressed in culture media near neutrality, especially when citric pectin is used as carbon source.…”

Section: Discussionmentioning

confidence: 99%

Differential expression ofplggenes fromPenicillium griseoroseum:plg1 a pectinolytic gene is expressed in sucrose and yeast extract

Bazzolli

Ribon

Reis

et al. 2008

Journal of Applied Microbiology

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Aims: To study the regulation of the plg1 and plg2 genes of Penicillium griseoroseum, in order to identify the industrial potential of their products in alternative carbon sources that are cheaper and widely available in Brazil. Methods and Results: RT-PCR and Northern blot were used to investigate if plg1 and plg2 expression is under influence of catabolic repression, ambient pH and cAMP. Results demonstrated that the genes were differentially regulated depending on the carbon sources in the culture medium and pH. Sucrose, a noninducing carbon source of the pectinolytic system, was able to promote plg1 transcription but only when yeast extract was added into the culture medium. Conclusions: The plg genes are differentially expressed. The plg1 gene is more attractive for industrial use due to its expression in alternative carbon sources like sucrose and yeast extract. Significance and Impact of the Study: In recent years, industries have been trying to replace the toxic conventional treatments employed in these processes by more eco-friendly enzyme treatment. Alternative carbon sources will be tested with the aim to reduce the costs associated to pectin lyase production in Brazil.

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A Second Pectin Lyase Gene(pel2) from Aspergillus oryzae KBN616. Its Sequence Analysis and Overexpression, and Characterization of the Gene Products.

Cited by 11 publications

References 11 publications

Cloning and characterization of a pectin lyase gene from Colletotrichum lindemuthianumand comparative phylogenetic/structural analyses with genes from phytopathogenic and saprophytic/opportunistic microorganisms

Cloning and characterization of a pectin lyase gene from Colletotrichum lindemuthianumand comparative phylogenetic/structural analyses with genes from phytopathogenic and saprophytic/opportunistic microorganisms

Production of Pectate Lyase byPenicillium viridicatum RFC3in Solid-State and Submerged Fermentation

Differential expression ofplggenes fromPenicillium griseoroseum:plg1 a pectinolytic gene is expressed in sucrose and yeast extract

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